Tyrosinase and Carbonic Anhydrase Enzymes Inhibition Studies of Vanadium(V) Complexes

Present study endeavors synthesis of series of vanadium(V) hydrazide complexes and its enzyme inhibition studies. Octahedral structure of complexes has been evaluated previously using conductance measurements, spectroscopic techniques involving IR, H-1-NMR and C-13-NMR, elemental analysis using CHN technique. Complexes 1c-12c have found to exhibit monomeric form with hydrazides behaving as bidentate ligand coordinating by their N and O atoms, while two oxygen atoms have also been found to show attachment with the metal centre. This study includes activity of vanadium(V) complexes to inhibit tyrosinase and carbonic anhydrase enzymes. For inhibition of carbonic anhydrase all, while for tyrosinase most of the hydrazide ligands were found to be inactive. Vanadium(V) complexes with these hydrazides have found to bear variable degree of carbonic anhydrase and tyrosinase inhibition activity. Some of the vanadium(V) hydrazide complexes were found to be potent inhibitors of tyrosinase enzyme and carbonic anhydrase as well.